Primary Information |
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BoMiProt ID | Bomi318 |
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Protein Name | Vitamin K-dependent protein C (Fragment) |
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Organism | Bos taurus |
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Uniprot ID | P00745 |
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Milk Fraction | Whey |
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Aminoacid Length | 456 |
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Molecular Weight | 51409 |
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FASTA Sequence |
Download |
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Gene Name | PROC |
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Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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Protein Function | vitamin-K-dependent plasma
zymogen; potently inhibits coagulation by
inactivating factors V and VIII, and it facilitates
fibrinolysis in vivo; Activated protein-C functions as an anticoagulant
by inactivating factor V and factor V1II; terminal
enzyme in the coagulation pathway and directly
responsible for factor V and VIII inactivation |
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Biochemical Properties | As found in humans and bovines, two-chain, disulfide-linked protein; thrombin activates human protein-C by a
single cleavage that appears to be between Arg 12 and
Leu 13 of the heavy chain which is inhibited at high physiologic Ca2+; The light chain contains ɣ-carboxyglutamic acid residues
that are involved in Ca2+-dependent membrane association;
light chain of bovine protein-C also contains
one residue of fl-hydroxyaspartic acid at position
71; Activated protein C and protein S form an anticoagulant complex on
cell surfaces that inactivates two of the regulatory proteins of
coagulation, factors Va and VIlla; |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Bibliography | 1. Kisiel, W. (1979) ‘Human Plasma Protein C’, Journal of Clinical Investigation, 64(3), pp. 761–769. doi: 10.1172/JCI109521. 2. Drakenberg, T. et al. (1983) ‘beta-Hydroxyaspartic acid in vitamin K-dependent protein C.’, Proceedings of the National Academy of Sciences, 80(7), pp. 1802–1806. doi: 10.1073/pnas.80.7.1802. 3. Vehar, G. A. and Davie, E. W. (1980) ‘Preparation and properties of bovine factor VIII (antihemophilic factor)’, Biochemistry, 19(3), pp. 401–410. doi: 10.1021/bi00544a001. |